ライフサイエンスコーパス: hemoprotein

1 the monooxygenase reaction catalyzed by this hemoprotein.

2 affinity of oxidized and reduced Pdx to the hemoprotein.

3 ytic degradation of the oxidatively modified hemoprotein.

4 of guanylate cyclase (sGC), a heterodimeric hemoprotein.

5 t, as in mammals, involves a redox-sensitive hemoprotein.

6 scherichia coli expressed purified HO-2 is a hemoprotein.

7 gests that oxygen tension may be sensed by a hemoprotein.

8 and a siroheme/Fe(4)S(4) cluster-containing hemoprotein.

9 p possess structural homology to a bacterial hemoprotein.

10 RmdA contains a PAS9 domain and is a hemoprotein.

11 ith the rate at which heme was lost from the hemoprotein.

12 to identify trends in the architecture of b hemoproteins.

13 , is similar to that of other monotyrosinate hemoproteins.

14 bility of these mutants to utilize hemin and hemoproteins.

15 ce have the potential to interact with human hemoproteins.

16 ns, which scavenge heme bound iron from host hemoproteins.

17 reliant on the acquisition of iron from host hemoproteins.

18 es efficient acquisition of Fe from heme and hemoproteins.

19 s reported for other six-coordinate NO-bound hemoproteins.

20 uired for assimilation of iron from heme and hemoproteins.

21 perone catalyzing the insertion of heme into hemoproteins.

22 terms of the axial His orientation in b-type hemoproteins.

23 fic for the heme in sGC versus that in other hemoproteins.

24 itochondria and cytoplasm, and deficiency of hemoproteins.

25 y employing mechanisms to utilize the host's hemoproteins.

26 only for the formation of cytochrome c-type hemoproteins.

27 is is thought to be reutilized from cellular hemoproteins.

28 ES is proposed for this remarkable family of hemoproteins.

29 hus enabling electron transfer between these hemoproteins.

30 ron porphyrin in each oxidation state of the hemoproteins.

31 uctural stability and enzymatic functions of hemoproteins.

32 ggests that ancestral CHI-like proteins were hemoproteins.

33 for CO-selective scavenging from endogenous hemoproteins.

34 ransfer as well as a structural component of hemoproteins.

35 r, host heme is sequestered in high-affinity hemoproteins.

36 LhaS accepted heme from diverse host-derived hemoproteins.

37 variety of biological functions mediated by hemoproteins.

38 g tyrosine common to the NEAT superfamily of hemoproteins.

39 tween the cell wall associated IsdA and IsdC hemoproteins.

40 stage without apparent dysfunction of major hemoproteins.

41 he selective ligand responses in gas-sensing hemoproteins.

42 sired effects when it is not incorporated in hemoproteins.

43 catalases, cytochromes, and other bacterial hemoproteins.

44 ates is in the form of heme as a cofactor of hemoproteins.

45 dicated to the acquisition of heme from host hemoproteins.

46 ct the regulation and physiology of cellular hemoproteins.

47 ized cytochrome P450s or by catalase-related hemoproteins.

48 avenge the essential nutrient iron from host hemoproteins.

49 in interactions between apoIsdC and upstream hemoproteins.

50 vide guidelines for the rational design of b hemoproteins: a modular structure including a packed, st

51 In one model, the putative hemoprotein adopts different conformational states depen

52 l rich in hemoglobin and/or other CO-binding hemoproteins, also contained substantial CO concentratio

53 HO-2 is a hemoprotein and binds heme at heme regulatory motifs (HR

54 have been shown to affect proper assembly of hemoprotein and decrease activity of the mutants express

55 ound that P. serpens lacks most of the known hemoproteins and does not require heme for electron tran

56 y the Cys-ligated hemes found in gas-sensing hemoproteins and in enzymes such as the cytochromes P450

57 Furthermore, during hyperoxia, lung hemoproteins and iron content were significantly increas

58 the catalytic boundaries of other oxidative hemoproteins and perform multiple functions.

59 Serratia marcescens, extracts heme from host hemoproteins and shuttles it to HasRSM, a specific hemop

60 revealing the ability of CO to bind to these hemoproteins and stimulate their binding at specific DNA

61 n IX complex, is a cofactor bound to various hemoproteins and supports a broad range of functions, su

62 ein in heme binding and utilization of serum hemoproteins and the HmuR YRAP motif in serum hemoprotei

63 Diatomic ligands in hemoproteins and the way they bind to the active center

64 standing of ultrareduced heme iron states in hemoproteins and their potential applications in biochem

65 he cell surface receptors IsdB and IsdH bind hemoproteins and transfer heme to IsdA, the final surfac

66 how the drug affects redox properties of the hemoprotein, and determined the 2.0 A X-ray structure of

67 h5 as the prototype of a new class of fungal hemoproteins, and emphasize the versatility of the Sec14

68 ption, the formation of hemoglobin and other hemoproteins, and iron recycling in macrophages.

69 he out-of-plane distortions of porphyrins in hemoproteins are characterized by displacements along th

70 Hemoproteins are critical for the function and integrity

71 Indeed, hemoproteins are found in almost every subcellular compa

72 Oxygenated hemoproteins are known to react rapidly with nitric oxid

73 Hemoproteins are powerful oxidative catalysts.

74 Hemoproteins are ubiquitous in biology and are commonly

75 While hemin, wild-type myoglobin, and other hemoproteins are unable to catalyze this reaction, the m

76 ment, as a heme auxotroph NTHi utilizes host hemoproteins as a source of essential iron.

77 nes, hmuRSTUV, required for use of hemin and hemoproteins as iron sources.

78 Group A streptococci (GAS) can use heme and hemoproteins as sources of iron.

79 The heme of hemoproteins, as exemplified by horseradish peroxidase (

80 rotein with the characteristic Soret band of hemoprotein at 424 nm.

81 ng subjects for evolutionary analysis of the hemoprotein-based oxygen-transport systems.

82 Hemoprotein-based scaffolds containing phosphorescent ru

83 nd-organ adverse effects compared with other hemoprotein-based therapeutics.

84 sidues of HmuR that may be involved in hemin/hemoprotein binding and utilization, we constructed a se

85 ing directed evolution, we have engineered a hemoprotein biocatalyst based on a thermostable cytochro

86 rr generates H2O2 from O2 as found for other hemoproteins, but H2O2 is less effective in oxidizing th

87 sGC and is a member of a family of conserved hemoproteins, called the H-NOX family (Heme-Nitric Oxide

88 Engineered hemoproteins can selectively incorporate nitrogen from n

89 heir readily tunable active-site geometries, hemoprotein "carbene transferases" could provide an alte

90 esis of beta-, gamma-, and delta-lactams via hemoprotein-catalysed intramolecular C-H amidation react

91 O-1, the first such intermediate observed in hemoprotein catalysis, completes our understanding of th

92 for both mechanistic analysis and design of hemoprotein-catalyzed carbene transfer reactions.

93 cDNAs in Escherichia coli, confirming their hemoprotein character.

94 mic resolution structure of the flavoprotein/hemoprotein complex, revealing how they interact in a mi

95 At higher doses, nitrosyl hemoprotein complexes could also be detected in liver ti

96 detected as nitrosyl hemoglobin or nitrosyl hemoprotein complexes in rats was the result of the meta

97 of Escherichia coli is an iron-mineralizing hemoprotein composed of 24 identical subunits, each cont

98 from bovine and rat lung is a heterodimeric hemoprotein composed of alpha1 and beta1 subunits.

99 e guanylate cyclase (sGC) is a heterodimeric hemoprotein composed of alpha1 and beta1 subunits.

100 s a heterodimeric, nitric oxide (NO)-sensing hemoprotein composed of two subunits, alpha1 and beta1.

101 The nature of the [Fe(IV)-O] center in hemoprotein Compounds II has recently received considera

102 techniques, we identify a family of dimeric hemoproteins comprising a domain of unknown function DUF

103 udy shows that in addition to calories, high hemoprotein concentrations in diving mammals necessitate

104 onal antibody raised against the recombinant hemoprotein confirmed primary expression of CYP2J2 prote

105 Another model proposes that the hemoprotein converts O2 to H2O2.

106 These findings with two monotopic ER hemoproteins, CYP2C11 and CYP3A4, and the polytopic ER p

107 The hepatic P450 hemoproteins CYPs 4A are typical N-terminally anchored t

108 tine in the active site of the monooxygenase hemoprotein cytochrome P450cam.

109 nt in each of the two major yeast CO-binding hemoproteins (cytochrome c oxidase and flavohemoglobin),

110 The transmembrane hemoprotein, cytochrome b(561) (b(561)), in the neuroend

111 agnetic resonance comparison of these ferric hemoproteins demonstrates that the mutation increases th

112 Here, we report engineered hemoproteins derived from a bacterial cytochrome P450 th

113 stantial extracellular heme is released from hemoproteins during hemorrhage and cell injury.

114 ve stress, suppressed coenzyme Q levels, and hemoprotein dysregulation.

115 50s) are endoplasmic reticulum (ER)-anchored hemoproteins engaged in the metabolism of numerous xeno-

116 itric-oxide synthase, a cytochrome P450-like hemoprotein enzyme, catalyzes the synthesis of nitric ox

117 Cytochromes P450 (P450s) are hemoprotein enzymes committed to the metabolism of chemi

118 for the function of several proteins termed "hemoproteins." Erythrocytes contain most of the body's h

119 Cytoglobin is a hemoprotein expressed in response to oxidative stress in

120 In the presence of heme or hemoproteins, expression of the bhuRSTUV operon is induc

121 ke proteins, introduces a new variation of a hemoprotein fold, and suggests that ancestral CHI-like p

122 ctivity in COS-1 cells, and minor amounts of hemoprotein for this mutant were expressed in E. coli an

123 lis, do not synthesize heme and rely on host hemoproteins for heme as a source of iron and protoporph

124 ent biocatalysts showcases the tunability of hemoproteins for highly selective functionalization of c

125 ssion increased the activity and quantity of hemoproteins found in several subcellular compartments,

126 and, in coral, by a 43-kDa catalase-related hemoprotein fused to the lipoxygenase that synthesizes t

127 We propose that deletion and disruption of hemoprotein genes in Asian noodlefishes and Antarctic ic

128 e first modified the designed helical bundle hemoprotein H4, creating a highly charged protein which

129 Hemoproteins have been recognized for nearly a century a

130 Hemoproteins have recently emerged as powerful biocataly

131 Hemoproteins have recently emerged as promising biocatal

132 Engineered hemoproteins have recently emerged as promising systems

133 heir presence and characterization in native hemoproteins have remained largely unexplored.

134 e report that S. aureus can utilize the host hemoproteins hemoglobin and myoglobin, but not hemopexin

135 he concentration and/or activity of cellular hemoproteins (hemoglobin, catalase, and cytochrome c oxi

136 s efficient acquisition of Fe from hemin and hemoproteins (hemoglobin, myoglobin, and catalase).

137 As a hemoprotein, hemoglobin (Hb) can, in the presence of H(2

138 Hemoproteins, hemoglobin and myoglobin, once released fr

139 coded by MB, is a small cytoplasmic globular hemoprotein highly expressed in cardiac myocytes and oxi

140 me-regulated eIF2alpha kinase (HRI) is a key hemoprotein in erythroid precursors that sense intracell

141 trate that cytoglobin is a stress-responsive hemoprotein in the hypoxia-induced hypertrophic myocardi

142 Cytochrome c is a multifunctional hemoprotein in the mitochondrial intermembrane space whe

143 in enhancing the catalytic efficiency of the hemoprotein in these reactions as well as modulating the

144 e tyrosine-liganded cAOS, a catalase-related hemoprotein in which a polyunsaturated fatty acid can en

145 heme can be transported and used in toto by hemoproteins in all six subcellular compartments examine

146 of the inflammatory response and binding to hemoproteins in order to restore homeostasis and sustain

147 oPPIX is directly incorporated into multiple hemoproteins in place of native heme b (FePPIX).

148 Plant alpha-dioxygenases (PADOX) are hemoproteins in the myeloperoxidase family.

149 It is demonstrated with the purified hemoproteins in vitro that the terminal oxidase can outc

150 nstrate in vitro that acetaminophen inhibits hemoprotein-induced lipid peroxidation by reducing ferry

151 orms use dietary heme for incorporation into hemoproteins, ingested heme is also used as an iron sour

152 Cytochrome c (cyt c) is a small hemoprotein involved in electron shuttling in the mitoch

153 Myeloperoxidase (MPO), the phagocyte hemoprotein involved in neutrophil host defense and cons

154 st that the redox state of an oxygen-binding hemoprotein is involved in controlling the expression of

155 igh-spin iron(II) than in low-spin iron(III) hemoproteins is attributed to the much stronger correlat

156 The nature of Fe-O2 bonding in hemoproteins is debated for decades.

157 Soluble guanylate cyclase (sGC), a hemoprotein, is the primary nitric oxide (NO) receptor i

158 nding sites, similar to that which occurs in hemoproteins, is achieved so that monodentate ligands ad

159 Upon release from the hemoproteins, it enters a biologically available state (

160 These sensors incorporate cytochrome c', a hemoprotein known to bind nitric oxide selectively.

161 ivity and normal hepatic microsomal heme and hemoprotein levels, they had 20% and 13% of wild-type ac

162 es share convergent or divergent patterns of hemoprotein loss, we sequenced the genomes of 11 species

163 ving the way to in vivo assembly of man-made hemoprotein maquettes and integration of artificial prot

164 PO and the novel mode of O(2) binding to the hemoprotein may provide important clues toward understan

165 e prooxidant effects of free iron, heme, and hemoproteins may be attributed to the formation of hyper

166 Hemoproteins may not be as stringent about the type of a

167 gy uncovers exciting possibilities as to how hemoproteins may participate in a range of physiologic s

168 yridine-functionalized cyclopropanes via the hemoprotein-mediated activation of pyridotriazoles (PyTz

169 The hemoprotein-mediated oxidation of carboxylic acids, ubiq

170 ions for acetaminophen in diseases involving hemoprotein-mediated oxidative injury.

171 orm alpha-helices when incorporated in novel hemoprotein model compounds, peptide-sandwiched mesoheme

172 (II)-O(2) is relatively high, in contrast to hemoprotein model compounds.

173 Five alkyne-containing hemoprotein models have been synthesized in a convergent

174 peptides may influence the properties of the hemoprotein models.

175 radical-derived DMPO nitrone adducts in the hemoprotein Mycobacterium tuberculosis catalase-peroxida

176 The hemoprotein myoglobin is a model system for the study of

177 Cytochromes P450 are monotopic hemoproteins N-terminally anchored to the ER membrane wi

178 obacterium Nostoc commune UTEX 584 encodes a hemoprotein, named cyanoglobin, that has high oxygen aff

179 These motifs and the hemoprotein nature of HO-3 suggest a potential regulator

180 cess of coupled oxidation of model hemes and hemoproteins not involved in heme catabolism, the corres

181 en known for some years that the reaction of hemoproteins, notably cytochrome P450, with PN leads to

182 eme-containing enzymes (NirBD), cytochrome c hemoproteins (NrfA and NirS), and copper-containing enzy

183 Neuroglobin is a highly conserved hemoprotein of uncertain physiological function that evo

184 uptake, mitochondrial heme, oxygen-utilizing hemoproteins, oxygen consumption, ATP generation, and ke

185 Cytochrome P450s are hemoprotein oxygenases involved in natural product synth

186 ng subcellular-targeted, genetically encoded hemoprotein peroxidase reporters, that both extracellula

187 Hemoproteins play central roles in the formation and uti

188 The ubiquitous cytochrome P450 hemoproteins play important functional roles in the meta

189 and eosinophil peroxidase (EPO), a secreted hemoprotein, plays a central role in oxidant production

190 classes for which mutant enzymes of natural hemoproteins previously reacted with low enantioselectiv

191 classes for which mutant enzymes of natural hemoproteins previously reacted with low enantioselectiv

192 b Hemoproteins provide multiple examples of this behavior.

193 limited by scavenging reactions with several hemoproteins, raising questions as to how free NO can si

194 O and ferrous heme, we hypothesized that the hemoprotein RcoM, a transcriptional regulator of microbi

195 The catalase-related hemoprotein reacted rapidly and specifically with linole

196 e of exploring the scope of catalase-related hemoprotein reactivity toward fatty acid hydroperoxides,

197 The chlorite dismutase family of hemoproteins received its name due to the ability of the

198 We evaluate the streptococcal hemoprotein receptor (Shr), a conserved streptococcal pr

199 le guanylate cyclase (sGC) is a ferrous iron hemoprotein receptor for nitric oxide (NO).

200 d therefore was named Shr, for streptococcal hemoprotein receptor.

201 SiaA and Shr are the first hemoprotein receptors identified in S. pyogenes; their p

202 h DPI under 21% O(2) and then exposed to the hemoprotein reductant sodium dithionite (1 mmol/L) under

203 f Fe starvation and the presence of heme (or hemoproteins), regulates P(bhuR), a heme-responsive prom

204 ng questions as to how free NO can signal in hemoprotein-rich environments.

205 kely to contribute to the reaction; and (iv) hemoprotein-rich tissues such as cardiac muscle are vuln

206 sinophil peroxidase (EPO), a highly cationic hemoprotein secreted by activation of eosinophils, is be

207 and that cytochrome c oxidase is likely the hemoprotein "sensor." Our findings also indicate that th

208 s the reduction of E. coli sulfite reductase hemoprotein (SiR-HP).

209 er of the Escherichia coli sulfite reductase hemoprotein (SiRHP) is exquisitely designed to catalyze

210 ed by the Escherichia coli sulfite reductase hemoprotein (SiRHP), we have determined crystallographic

211 ha subunit) and the other an iron-containing hemoprotein (SiRHP, the beta subunit), assemble to make

212 a physiologically relevant activator of the hemoprotein soluble guanylate cyclase (sGC).

213 ogically relevant activator of the mammalian hemoprotein soluble guanylate cyclase (sGC).

214 HO-2, is a poor heme catalyst, and displays hemoprotein spectral characteristics.

215 The active site, found in the hemoprotein subunit (SiRHP), sits on the distal face of

216 te reductase shows a broad similarity to the hemoprotein subunit of sulfite reductase but has many si

217 rmediate succinyl CoA for incorporation into hemoproteins, such as the cytochromes needed for oxidati

218 here show that Gyc-88E from Drosophila is a hemoprotein that binds oxygen, as well as NO and CO.

219 e guanylate cyclase (sGC) is a heterodimeric hemoprotein that catalyzes the conversion of GTP to cGMP

220 oxide synthase (NOS) is a homodimeric flavo-hemoprotein that catalyzes the oxidation of L-arginine t

221 sGC is a heterodimeric hemoprotein that contains a Heme-Nitric oxide and OXygen

222 clase (sGC) is a nitric oxide- (NO-) sensing hemoprotein that has been found in eukaryotes from Droso

223 Aromatase, a cytochrome P450 hemoprotein that is responsible for estrogen biosynthesi

224 We also report a novel form of the hemoprotein that occurs in the absence of its cofactors.

225 Myeloperoxidase (MPO), a hemoprotein that uses H(2)O(2) as the electron acceptor

226 Nitric oxide synthases (NOS) are hemoproteins that catalyze the reaction of L-arginine to

227 e prostate (STEAP) 1-4 are membrane-embedded hemoproteins that chelate a heme prosthetic group in a t

228 e de novo, even though these animals contain hemoproteins that function in key biological processes.

229 ies similar to those of cytochrome P450-type hemoproteins that have undergone conversion to the catal

230 Heme b is an iron-containing cofactor in hemoproteins that participates in the fundamental proces

231 erfamily of genes encoding mostly microsomal hemoproteins that play a dominant role in the metabolism

232 c heme levels produces phenotypic changes in hemoproteins that protect cells from certain stresses.

233 lian nitric oxide synthases (NOSs) are flavo-hemoproteins that rely on dynamic interdomain interactio

234 In contrast to typical hemoproteins, the protein surface is not directly access

235 is typical for O(2) binding to other ferrous hemoproteins, the reaction involves several kinetically

236 mic factors that determine the assembly in b hemoproteins, the solution structure of the 98-residue p

237 ase (MPO) is an abundant mammalian phagocyte hemoprotein thought to primarily mediate host defense re

238 a strategy that expands the functionality of hemoproteins through orthogonal enzyme/heme pairs.

239 study highlights the potential of engineered hemoproteins to access natural nitrogen sources for sust

240 The ability of hemoproteins to catalyze epoxidation or hydroxylation re

241 urface proteins contribute to the binding of hemoproteins to S. pyogenes.

242 ialized cytochromes P450 or catalase-related hemoproteins transform fatty acid hydroperoxides to alle

243 50 monooxygenases (termed CYPs or P450s) are hemoproteins ubiquitously found across all kingdoms, pla

244 and is required for utilizing hemin and all hemoproteins under iron-depleted conditions.

245 ococcus aureus scavenges heme-iron from host hemoproteins using iron-regulated surface determinant (I

246 In this study, we investigate hemoprotein utilization by S. pyogenes.

247 vium expresses, in addition to the BhuR heme/hemoprotein utilization system, an alternative RhuR-inde

248 emoproteins and the HmuR YRAP motif in serum hemoprotein utilization.

249 requirement by obtaining heme iron from host hemoproteins via IsdG- and IsdI-mediated heme degradatio

250 protein has revealed the first example of a hemoprotein which can utilize both sides of its heme (di

251 losoxidans cytochrome c', a mono-His ligated hemoprotein which reversibly binds NO and CO but not O(2

252 soluble form of guanylate cyclase (sGC) is a hemoprotein which serves as the only known receptor for

253 Heme is essential to the function of hemoproteins, which are involved in energy generation by

254 ctivation of the peroxynitrite anion (PN) by hemoproteins, which leads to its detoxification or, on t

255 ) was comparable to that observed with other hemoproteins whose activities are thought to be modulate

256 HRI is a hemoprotein with 2 distinct heme-binding domains.

257 elements that discriminate between pairing a hemoprotein with a diflavin reductase, as in the E. coli

258 ctra showed that TXAS was a typical low spin hemoprotein with a proximal thiolate ligand and had a ve

259 ells correlated with decreased expression of hemoprotein with a reduced difference spectrum of 450 nm

260 ox-active penta-coordinate high spin Fe(III) hemoprotein with an unusual heme-binding arrangement tha

261 encoding a fusion protein of a catalase-like hemoprotein with an unusually short LOX (approximately 4

262 8R-lipoxygenase in Plexaura homomalla, is a hemoprotein with sequence similarity to catalases.

263 We found that HRI purified as a hemoprotein with the characteristic Soret band of hemopr

264 Coral allene oxide synthase (AOS), a hemoprotein with weak sequence homology to catalase, is

265 Hemoproteins with this type of engineered cofactor have